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Database: UniProt
Entry: A0A084VHY6_ANOSI
LinkDB: A0A084VHY6_ANOSI
Original site: A0A084VHY6_ANOSI 
ID   A0A084VHY6_ANOSI        Unreviewed;       676 AA.
AC   A0A084VHY6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN   ORFNames=ZHAS_00004820 {ECO:0000313|EMBL:KFB37580.1};
OS   Anopheles sinensis (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB37580.1};
RN   [1] {ECO:0000313|EMBL:KFB37580.1, ECO:0000313|Proteomes:UP000030765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA   Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA   Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA   Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT   "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT   of mosquito competence for malaria parasites.";
RL   BMC Genomics 15:42-42(2014).
RN   [2] {ECO:0000313|EnsemblMetazoa:ASIC004820-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC         phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001031};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC       glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-
CC       fructose 6-phosphate: step 1/1. {ECO:0000256|ARBA:ARBA00004775}.
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DR   EMBL; ATLV01013250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KE524847; KFB37580.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084VHY6; -.
DR   STRING; 74873.A0A084VHY6; -.
DR   EnsemblMetazoa; ASIC004820-RA; ASIC004820-PA; ASIC004820.
DR   VEuPathDB; VectorBase:ASIC004820; -.
DR   VEuPathDB; VectorBase:ASIS023477; -.
DR   OMA; EWYLASD; -.
DR   UniPathway; UPA00113; UER00528.
DR   Proteomes; UP000030765; Unassembled WGS sequence.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00714; GFAT; 1.
DR   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR005855; GFAT.
DR   InterPro; IPR047084; GFAT_N.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   NCBIfam; TIGR01135; glmS; 1.
DR   PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1.
DR   PANTHER; PTHR10937:SF0; GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING); 1.
DR   Pfam; PF13522; GATase_6; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030765};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..282
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          354..494
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          525..666
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   676 AA;  75402 MW;  2D588C4F7244778A CRC64;
     MCGIFAYLNF LTPKSRREVL ELLLNGLKRL EYRGYDSAGV AVDGIAADAG ILLFKRTGKV
     KVLEDAIREA AKEIDFSEAC DTHVGIAHTR WATHGAPSEL NSHPQRSDDT NAFVVVHNGI
     VTNYKDIKKF LELRGYSFES DTDTETIAKL VHHLWKQHPN YSFRELVEQV IQQLEGAFAL
     AFKSKHFPGE CVVTRRGSPL LVGIKAKTSL ATNHVPILYG KGPRHGSLGN VQVEPTPDNT
     ADFINPGEEV EYFFASDASA VIEHTNRVIY LEDDDVAAVK DGALGIHRLK KSLDDPHARE
     ITTLKMEIQQ IMKGNYRYFM QKEIFEQPES VVNTMRGRVN FDSKKVTLGG IKDYIPEIKR
     CRRLMLIACG TSYHSAVATR QLLEELTELP VMVELASDFL DRNTPIYRDD VCFFISQSGE
     TADTLMALRY CKQRGALIVG ITNTVGSSIC RESHCGVHVN AGPEIGVAST KAYTSQFISL
     VMFALVMSED RLSLQSRRLE IIEGLRNLDA HIKQVLQLDQ KVLEIAQDLY QQKSLLIMGR
     GFNFATCMEG ALKVKELTYM HSEGIMAGEL KHGPLALVDD TMPIVMIIMR DPVHLKCMNA
     LQQVTAREGR PIIICEEGDN ETMAFASKAL EIPRTVDCLQ GVLTVIPMQL LSYHIAVLRG
     CNVDCPRNLA KSVTVE
//
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